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Journal article

A binary arginine methylation switch on histone H3 Arginine 2 regulates its interaction with WDR5

Authors : Lorton, Benjamin M; Harijan, Rajesh K; Burgos, Emmanuel S (2020)

Using highly accurate quantitative binding analysis combined with high-resolution crystal structures of WDR5 in complex with unmodified (me0) and me1/me2s L-Arginine amino acids and in complex with H3R2me1 peptide, we provide a rigorous biochemical study of this important biological interaction. Despite modest structural differences at the binding interface, our study supports an interaction model regulated by a binary arginine methylation switch: H3R2me2a prevents int...

Periodicals (Báo – Tạp chí)

Mechanism-based inhibitors of SIRT2: structure–activity relationship, Xray structures, target engagement, egulation of a-tubulin acetylation and inhibition of breast cancer cell migration†

Authors : Nielsen, Alexander L. (2020)

Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues. It affects diverse biological functions in the cell and has been considered a drug target in relation to both neurodegenerative diseases and cancer. Therefore, access to well-characterized and robust tool compounds is essential for the continued investigation of the complex functions of this enzyme. Here,&...

Periodicals (Báo – Tạp chí)

Structural insights on the substrate-binding proteins of the Mycobacterium tuberculosis mammalian-cell-entry (Mce) 1 and 4 complexes

Authors : Asthana, Pooja (2020)

Report the properties of the substrate-binding proteins (SBPs; MceA-F) of the Mce1 and Mce4 complexes from Mtb which are responsible for the import of mycolic acid/fatty acids, and cholesterol respectively. MceA-F are composed of four domains namely, transmembrane, MCE, helical and tail domains. Our studies show that MceA-F are predominantly monomeric when purified individually and do not form homohexamers unlike the reported homologs (MlaD, PqiB and Let...